If you have been reading about epitalon and want a single page that covers the useful parts, this is it: definitions, context, how it is studied, and the questions that come up repeatedly.
Last reviewed on 2026-03-14. Where a claim depends on a specific study, the study is described rather than over-claimed.
Laboratory-grade epitalon is typically supplied as a lyophilized powder. Purity is commonly assessed with reverse-phase high-performance liquid chromatography, often paired with mass spectrometry to confirm molecular identity. Amino acid analysis and peptide mapping can provide additional confirmation of sequence. Certificates of analysis for research materials frequently report purity above 95 percent, although the methods behind such figures vary between suppliers. The absence of a pharmacopeial monograph means that no single standardized assay defines the compound, so reported results depend on the analytical protocol chosen.
Storage recommendations center on limiting moisture, heat, and light. The dry powder is generally kept at minus 20 degrees Celsius, and some suppliers recommend minus 80 degrees for long-term archival. Once dissolved, solutions are usually aliquoted and frozen to avoid repeated freeze-thaw cycles, which can promote aggregation or degradation. Aqueous stability depends on pH and concentration, and buffered saline is often preferred over plain water for biological work. Stability data specific to epitalon remain limited, so general peptide-handling practices are applied by analogy rather than from product-specific validation.
Epitalon is a synthetic tetrapeptide with the sequence alanine-glutamate-aspartate-glycine, abbreviated AEDG. Its molecular formula is C14H22N4O9 and its calculated monoisotopic mass is approximately 390.35 daltons. The compound does not occur naturally as a free peptide; it is produced by solid-phase peptide synthesis. Because it contains two acidic residues and no basic residues, the neutral form carries a net negative charge at physiological pH. This charge profile influences how the peptide behaves in solution and during chromatographic analysis.
Epitalon is a synthetic tetrapeptide whose sequence is alanine–glutamate–aspartate–glycine, commonly abbreviated AEDG. It was developed in Russia during the 1980s and 1990s by investigators associated with the St. Petersburg Institute of Bioregulation and Gerontology, who studied short peptides as regulators of gene expression and tissue function. The alternative spelling epithalon appears interchangeably in the literature, and the two names refer to the same molecule. Outside Russia it is encountered chiefly as a research chemical rather than a licensed medicine, and it holds no approval from the United States Food and Drug Administration or the European Medicines Agency.
The peptide is a synthetic analogue of epithalamin, a preparation extracted from bovine pineal glands. Investigators sought a short, chemically defined molecule that would reproduce some of the endocrine and gerontological observations attributed to the glandular extract. Proposed mechanisms centre on induction of telomerase activity, an effect reported in cultured human somatic cells in the early 2000s, together with influences on melatonin secretion and neuroendocrine regulation. Those mechanisms remain incompletely characterised, and the reported telomerase response has not been consistently reproduced by independent groups working in comparable systems.
Published work on this compound consists mainly of in vitro experiments, animal studies, and small clinical investigations, a substantial share of which appeared in Russian-language journals. Sample sizes are generally small, control conditions differ between studies, and several endpoints rely on markers whose clinical meaning is itself debated. Reviews of the longevity field treat the peptide as an early example of telomerase-directed research rather than an established intervention. Regulatory treatment varies by country: some jurisdictions place it under prescription controls, others treat it as a laboratory material, and importation may be restricted regardless of local status.
| Property | Value | Notes |
|---|---|---|
| Molecular formula | C14H22N4O9 | Free acid form of the tetrapeptide |
| Molecular mass | About 390.35 Da | Calculated monoisotopic value |
| Appearance | White to off-white powder | Typical lyophilized presentation |
| Solubility | Soluble in water | Also dissolves in buffered saline |
| Storage temperature | Minus 20 degrees Celsius | Dry, dark conditions; avoid repeated thawing |
Literature searches for this compound must account for several spelling variants. Indexing databases contain epitalon, epithalon, epithalone, and AEDG, and relevant records are scattered across Russian-language and English-language journals that do not consistently cross-cite. Early publications describe the parent extract as a mixture of many peptides, whereas later work addresses the single synthetic tetrapeptide. That shift in nomenclature complicates comparison between studies, because extract data and tetrapeptide data are sometimes cited interchangeably. A search strategy omitting the alternate spellings will return an incomplete set of references.
Reported biological findings come mainly from cell culture and rodent experiments. Those studies describe changes in telomerase catalytic subunit expression, melatonin rhythm amplitude, and antioxidant enzyme activity after peptide exposure. Human data are sparse and consist of small trials with limited blinding and inconsistent endpoints. The proposed mechanisms remain hypotheses rather than established facts, and there is no consensus on whether effects observed in animals carry over to people. Independent replication outside the original research groups is limited, which is a recognised gap in the published literature.
The parent extract epithalamin was characterised as a low-molecular-weight fraction of pineal tissue rather than a single defined chemical entity. Researchers fractionated it and tested successive fragments for activity, a screening approach typical of peptide discovery work in that era. Epitalon emerged from that process as one of the shorter sequences of interest. Because the original extract was never fully resolved into individual components, claims about which constituent drives a given effect rest on inference. This distinction matters when reading older reports that attribute extract observations to the tetrapeptide itself.
Most experimental work has been carried out in cell culture and animal models. Several reports describe changes in telomerase activity and proliferation in cultured cells, while rodent studies have examined lifespan, melatonin rhythm and reproductive endpoints. Human data remain limited, and much of the published clinical material consists of small trials with incomplete reporting of methods and controls. Whether the cell and animal findings translate into measurable effects in people is an open question, and the mechanistic basis of the reported telomerase changes is not fully established.
Discussions in the literature often conflate three distinct entities: the pineal extract epithalamin, the isolated tetrapeptide AEDG, and commercial preparations sold under similar names. Reviews citing older Russian-language studies sometimes omit detail on purity, route of administration and control groups, which makes cross-study comparison difficult. Researchers working with the compound generally note the need for independent replication, standardized enzyme assays, and clearer reporting of peptide identity. These caveats are relevant when weighing claims that appear in secondary sources rather than in primary reports.
Residue composition is the property that most cleanly separates verified material from mislabelled samples. Alanine, glutamate, aspartate and glycine appear in that order from the N-terminus, and the two acidic residues sit in the middle of the chain. Because the peptide is short, it can be produced by solid-phase synthesis and characterised by mass spectrometry without ambiguity. Any reported sample whose measured mass departs substantially from 390 daltons is a different compound or a degraded mixture rather than epitalon.
Epitalon is a synthetic tetrapeptide whose four residues are alanine, glutamate, aspartate and glycine, commonly abbreviated AEDG. Its molecular formula is C14H22N4O9 and its monoisotopic mass is near 390.35 daltons. The peptide carries two acidic side chains, so it is neutral to negatively charged in most aqueous buffers. Published reference summaries usually list it under both spellings, epitalon and epithalon, and treat the two names as the same material.
The compound is generally described as a synthetic analogue of a fragment isolated from a pineal gland extract. Researchers associated with the Saint Petersburg Institute of Bioregulation and Gerontology introduced it during the 1980s and 1990s while studying short peptides from animal tissue. The original extract, called epithalamin, is a heterogeneous mixture, whereas epitalon is a single defined sequence. That distinction matters because findings reported for the extract are not automatically findings about the pure tetrapeptide, and claims about broader biological effects remain a separate question from the chemical identity described here.
Transparency of information is another factor defining a delivery system. Access to information on conditions, treatments, quality, and pricing greatly affects the choice of patients/consumers and, therefore, the incentives of medical professionals. While the US healthcare system has come under fire for its lack of openness, new legislation may encourage greater openness. There is a perceived tension between the demand for transparency and concerns over patient confidentiality and the commercial misuse of medical data. Advocates argue that openness helps patients make informed decisions, while critics warn it can expose sensitive records and invite exploitation by insurers, employers, or marketers. Balancing accountability with privacy remains a central challenge. The health professionals who provide care in medicine comprise multiple professions, such as medics, nurses, physiotherapists, and psychologists. These professions will have their own ethical standards, professional education, and bodies. The medical profession has been conceptualized from a sociological perspective.
=== Pharmacokinetics === There have been several clinical studies to examine the pharmacokinetics of deramciclane, which can readily cross the blood–brain barrier. Overall, studies show that deramciclane follows linear pharmacokinetics in humans with oral daily doses ranging from 3–150 mg and twice daily doses ranging from 10–60 mg. Additionally, no differences have been found in adsorption, distribution, metabolism, or elimination when an oral dose is administered in tablet or capsule form. Deramciclane is rapidly absorbed from the gastrointestinal tract. Studies show that the drug can be detected in plasma as quickly as 20 minutes after dosing. Deramciclane demonstrates a Tmax of 2–4 hours and is unaffected by dosage. The Cmax at this time is approximately 140 ng/mL. A typical PTF (peak trough fluctuation) is 70-80% over four weeks of administration, and is unaffected by dose. The oral tablet of deramciclane yields a bioavailability of 36% on average, which is considered decent enough for oral administration and avoid the necessity of a more invasive route. The pharmacokinetics of deramciclane are also studied in rats, mice, rabbits, and dogs. Rat and rabbits show the fastest metabolism rates of the drug, and dogs are the only animals to show non-linear pharmacokinetics of deramciclane. Phase I metabolism in rat hepatocytes is similar enough to that in humans that the rat can be used as a predictive model for human metabolism of deramciclane. In rats, the Tmax is found to be 0.5 hours after a single 10 mg/kg dose and the half-life of deramciclane is about 3.5-5.5 hours.
S = Salt factor F = Bioavailability D = Dose ke = Elimination rate constant ka = Absorption rate constant Vd = Volume of distribution τ = Dosing interval Cmin is also an important parameter in bioavailability and bioequivalence studies, it is part of the pharmacokinetic information recommended for submission of investigational new drug applications.
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A membrane transport protein is a membrane protein involved in the movement of ions, small molecules, and macromolecules such as another protein, across a biological membrane. Transport proteins are integral transmembrane proteins, that is: they exist permanently within and span the membrane, across which they transport substances. The proteins may assist in the movement of substances by facilitated diffusion, active transport, osmosis, or reverse diffusion. The two main types of proteins involved in such transport are broadly categorized as either channels or carriers (a.k.a. permeases or transporters). Examples of channel/carrier proteins include the GLUT 1 uniporter, sodium channels, and potassium channels. The solute carriers and atypical SLCs are secondary active or facilitative transporters in humans. Collectively membrane transporters and channels are known as the transportome. Transportomes govern cellular influx and efflux of, not only ions and nutrients, but drugs as well.
Since the bacteriophage Phage Φ-X174 was sequenced in 1977, the DNA sequences of thousands of organisms have been decoded and stored in databases. This sequence information is analyzed to determine genes that encode proteins, RNA genes, regulatory sequences, structural motifs, and repetitive sequences. A comparison of genes within a species or between different species can show similarities between protein functions, or relations between species (the use of molecular systematics to construct phylogenetic trees). With the growing amount of data, it long ago became impractical to analyze DNA sequences manually. Computer programs such as BLAST are used routinely to search sequences—as of 2008, from more than 260,000 organisms, containing over 190 billion nucleotides. Before sequences can be analyzed, they are obtained from a data storage bank, such as GenBank. DNA sequencing is still a non-trivial problem as the raw data may be noisy or affected by weak signals. Algorithms have been developed for base calling for the various experimental approaches to DNA sequencing.
2023 Analytical Scientist the Power List - Leaders and Advocates 2020 Society for Glycobiology Molecular and Cellular Proteomics (MCP) / American Society for Biochemistry and Molecular Biology (ASBMB) Lectureship Award 2019 inaugural winner of the US Human Proteome Organization Lifetime Achievement in Proteomics Award 2019 Analytical Scientist the Power List 2017 American Society for Mass Spectrometry John B. Fenn Award for a Distinguished Contribution in Mass Spectrometry 2016 American Association for the Advancement of Science Fellow 2015 Human Proteome Organization Distinguished Service Award 2015 German Mass Spectrometry Society (Deutsche Gesellschaft für Massenspektrometrie, DGMS) Wolfgang Paul Lecture 2013 Boston University The William Fairfield Warren Distinguished Professorship 2011 American Chemical Society Fellow 2010 American Chemical Society Frank H. Field and Joe L. Franklin Award for Outstanding Achievement in Mass Spectrometry 2009 International Mass Spectrometry Foundation Thomson Medal 2008 Human Proteome Organization Discovery in Proteomic Sciences Award
Sources: en.wikipedia.org
=== 2010-2013 === In 2010, Janusz Bugajski argued that Vladimir Putin and Dmitry Medvedev "were convinced that Europe and the United States needed Russia much more than Russia needed the West and calculated that several tangible advantages would be gained from the military attack on Georgia". In 2011, Michael Cecire explained that "citations of ’US training’ to Georgian troops have limited relevance in the context of the August war" since Americans trained Georgians for fighting with the insurgents and not for the war with Russia. Cecire further states: "The absence of Georgia's best troops has also been cited as being one of the clearest signs that Tbilisi did not have a premeditated intention to get into a war, and certainly not one with the Russian military. [...] Many observers agree that even if Georgia did premeditate the August 2008 war (and that is a big if), it was not counting on Russian involvement". In 2011, Dr. Ariel Cohen and Colonel Robert E. Hamilton wrote, "The Vladimir Putin-Dmitry Medvedev administration and the defense establishment formulated far-reaching goals when they carefully prepared over 2 1/2 years for a combined operations-style invasion of Georgia.
Chapter 1: Continuous Population Models for Single Species Chapter 2: Discrete Population Models for a Single Species Chapter 3: Models for Interacting Populations Chapter 4: Temperature-Dependent Sex Determination (TSD) Chapter 5: Modelling the Dynamics of Marital Interaction: Divorce Prediction and Marriage Repair Chapter 6: Reaction Kinetics Chapter 7: Biological Oscillators and Switches Chapter 8: BZ Oscillating Reactions Chapter 9: Perturbed and Coupled Oscillators and Black Holes Chapter 10: Dynamics of Infectious Diseases Chapter 11: Reaction Diffusion, Chemotaxis, and Nonlocal Mechanisms Chapter 12: Oscillator-Generated Wave Phenomena Chapter 13: Biological Waves: Single-Species Models Chapter 14: Use and Abuse of Fractals
Light and temperature impact the speed of deterioration, especially in combination with other agents of decay. Exposure of any length to light causes fading. Light both visible and UV can bleach and dry textiles as well as fade color. It is recommended that light is kept at 50 lux for textiles while on display. The length of exposure to light is determined by the type of textile and the object's current condition. Physical agents of decay include the natural breakdown of biological material, which causes fabrics to become more brittle as they age. Humidity is a factor that impacts textile fibers. Loss of moisture decreases the elasticity and increases brittleness. An environment that is too humid encourages pest activity and the growth of mold. Pests affect the physical makeup of textiles by eating fibers, and this destabilizes the fabrics. Pest activity can also discolor materials. Mold weakens and stains textiles. Chemical deterioration of textiles is caused by a variety of interactions. For example, the interaction of fibres with metals, pollutants, adhesives and other even other fibers can cause deterioration. Oxidation of metal threads or adornments can discolor and tarnish textiles due to the chemical reaction between the oxygen in the air and the fibers. Pollution impacts textiles. Pollution can come from the environment or the actual textile manufacturing process. These pollutants include pollen, mold, skin cells, ash, dirt and metal dust. Sources can include the museum exhibit and storage materials and air coming in from outside the museum.
== Activating and inhibiting agents == The SC-FAs that activate FFAR3 include proprionic, butyric, acetic, valeric caproic, and formic acids. (Confusingly, butyric acid also activates hydroxycarboxylic acid receptor 2 and β-hydroxybutyric acid has been reported to stimulate or inhibit FFAR3.) FFAR2 is activated by many of these same SC-FAs but differs from FFAR3 in its relative binding affinities for them. In humans, the binding affinity ranking of FFAR3 is: propionic = butyric = valeric > acetic > formic acids (acetic and formic acids have very low binding affinities for, and therefore must be at extremely high levels to activate, FFAR3); FFAR2's relative binding affinity ranking for these SC-FAs is: acetic = propionic > butyric > valeric = formic acids. AR420626 (a derivative of an older compound 1-MCPC) has been reported to be a selective activator of FFAR3 but has also been reported to inhibit the activation of FFAR3. Its actions require further characterizations. AR399519 and CF3-MQC have been reported to inhibit the activation of mouse FFAR3; the actions of these agents also require further characterizations.
Sources: en.wikipedia.org
Epitalon is a synthetic tetrapeptide built from four amino acids: alanine, glutamate, aspartate, and glycine. It is not extracted from a natural source but made in the laboratory by chemical synthesis. Its short length makes it relatively straightforward to produce at high purity.
No naturally occurring free form of the peptide has been described. The four-amino-acid sequence can appear as a fragment within larger proteins, but that is not the same as the intact compound being present as a circulating molecule. Materials used in research are synthetic.
Purity is usually checked by reverse-phase high-performance liquid chromatography, which separates the target peptide from related impurities. Mass spectrometry is commonly used alongside it to confirm molecular mass. Some suppliers also provide amino acid analysis for additional sequence confirmation.
Epitalon is a synthetic four-amino-acid peptide with the sequence alanine–glutamate–aspartate–glycine, also written AEDG. It was developed in Russian gerontology research and is studied for proposed effects on telomerase, melatonin regulation, and neuroendocrine function. It is not an approved pharmaceutical in the United States or the European Union.